Steady state and time-resolved IR spectroscopy of the native and unfolded states of bovine ubiquitin: protein stability and temperature-jump kinetic measurements of protein folding at low pH

  • Colley C
  • Griffiths-Jones S
  • George M
 et al. 
  • 19


    Mendeley users who have this article in their library.
  • 16


    Citations of this article.


Infrared spectroscopy has been used to characterise the folded and unfolded states of bovine ubiquitin (a small protein of 76 residues) under acidic conditions (pH 1); fast time-resolved measurements of protein unfolding, initiated by a laser-induced temperature-jump of 8 °C, shows rapid refolding and β-sheet secondary structure formation on a timescale of a few milliseconds.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Get full text


  • Christopher S. Colley

  • Samuel R. Griffiths-Jones

  • Michael W. George

  • Mark S. Searle

  • Ian P. Clark

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free